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MolNFT v1 · #114146 · protein

Homo-dimeric structure of cytochrome C' from thermophilic hydrogenophilus thermoluteolus

5B3I · Cytochrome C prime: “Homo-dimeric structure of cytochrome C' from thermophilic hydrogenophilus thermoluteolus”. X-ray diffraction, 1 ligand (HEC), 8 pockets (best druggability 0.79). MolNFT v1 #114146 on GenesisL1: 3D structure…

PDB
5B3I
Type
protein
Length
540 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C prime
UniProt
F7J213
Ligands
HEC
Pockets
8 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCytochrome C primeprotein13573% helix, 3% strandF7J213

Ligands and binding sites

  • HEC · Heme C · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17950.790.8277HEC
24420.760.8551HEC
34210.720.8243HEC
44220.720.8245HEC
51650.450.7523empty

Interfaces

5 interfaces between chains.

  • A–B · 965 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 946 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 326 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 25 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 16 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 cofactor (heme c attachment).

Compared structures

  • 5B3I · Homo-dimeric structure of cytochrome c' from Thermophilic Hydrogenophilus thermoluteolus · the same entry in another collection · chain A against A, TM-score 1.00

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